Food-derived proteins as the source of sensory peptides based on computer prediction

Hydrolysis of food proteins contributes to the release of biologically and functionally active peptides, including sensory (tastant) sequences. The latter are considered by consumers as undesired, especially when thinking about protein hydrolysates being the components of e.g. functional food. The aim of the study was the computer analysis of food-derived protein sequences being potential source of tastant peptides. Analyses included the following steps: elaboration of the profiles of potential sensory activity of proteins as well as the computer simulation of hydrolysis of proteins to generate tastant/bioactive peptides. The selected plant and animal protein sequences (derived from oil and leguminous plants, crops, milk, fish, and meat) were taken for the bioinformatics analysis using the sub-database of sensory peptides and amino acids – BIOPEP-UWM available at: https://biochemia. uwm.edu.pl/biopep-uwm [as of February 2023]. The profile of potential sensory activity of protein was defined as the location and type of sensory peptide(s) in a protein chain. The computer simulation of hydrolysis of proteins was performed using endopeptidases acquired from BIOPEP-UWM database. The results revealed that majority of peptides located in protein sequences were bitter. Moreover, the largest number of bitter peptides was present in milk and carp proteins (caseins and myosin, respectively). Ficin and papain potentially released the largest number of tastant peptides from all proteins analysed. Some peptide tastants revealed biological potential as the dietary components supporting the metabolic syndrome prophylaxis. Our studies confirmed the suitability of selected bioinformatics tools in studying the proteins as the food components being the source of tastant/bioactive peptides.